|
Name |
Accession |
Description |
Interval |
E-value |
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
14-290 |
1.71e-97 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 288.63 E-value: 1.71e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 14 AAIGLLWCASALLAETGETSAQTARLISVDGAITEILYALGGEAQLVGVDTTSLYPDATEDIAKVGYKRALSAEGILSLN 93
Cdd:COG4558 5 ALALLLLALAALAAGASVAAAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGILSLK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 94 PDRLLMTDDAGPPEVLEQIARAGVDTHPIPDTPSVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATERSSKRP 173
Cdd:COG4558 85 PTLVLASEGAGPPEVLDQLRAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAAIGKPP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 174 RLLFLLHIGSGNDMAAGRDTAADTVIRLAGGENVLhDAFSGYKPLSAEAALAAAPEVILVTQRNLEQLGGLDAVLERGAL 253
Cdd:COG4558 165 RVLFLLSRGGGRPMVAGRGTAADALIRLAGGVNAA-AGFEGYKPLSAEALIAAAPDVILVMTRGLESLGGVDGLLALPGL 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 1957874216 254 QATPAGQARRVLAMDGPLLLAFGPRLAVAAAQLASEL 290
Cdd:COG4558 244 AQTPAGKNKRIVAMDDLLLLGFGPRTPQAALALAQAL 280
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
38-269 |
2.80e-70 |
|
Hemin binding protein HutB. These proteins have been shown to function as initial receptors in ABC transport of hemin and hemoproteins in many eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238569 [Multi-domain] Cd Length: 235 Bit Score: 217.52 E-value: 2.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 38 RLISVDGAITEILYALGGEAQLVGVDTTSLYPDATEDIAKVGYKRALSAEGILSLNPDRLLMTDDAGPPEVLEQIARAGV 117
Cdd:cd01149 3 RIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEALDQLRAAGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 118 DTHPIPDTPSVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATERSSKRPRLLFLLHIGSGNDMAAGRDTAADT 197
Cdd:cd01149 83 PVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVLFLLSHGGGAAMAAGRNTAADA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1957874216 198 VIRLAGGENVLhDAFSGYKPLSAEAALAAAPEVILVTQRNLEQLGGLDAVLERGALQATPAGQARRVLAMDG 269
Cdd:cd01149 163 IIALAGAVNAA-AGFRGYKPLSAEALIAAQPDVILVMSRGLDAVGGVDGLLKLPGLAQTPAGRNKRILAMDD 233
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
40-268 |
4.90e-28 |
|
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 426291 [Multi-domain] Cd Length: 233 Bit Score: 108.22 E-value: 4.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 40 ISVDGAITEILYALGGEAQLVGVDTTSLYP---DATEDIAKVGYKRALSAEGILSLNPDRLLMtDDAGPPEVLEQIARAG 116
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPlkaDAVAAIVKVGAYGEINVERLAALKPDLVIL-STGYLTDEAEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 117 VDTHPIPDTPSVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATERSSKRPRLLFLLHIGSGNdMAAGRDTAAD 196
Cdd:pfam01497 80 IPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGY-VVAGSNTYIG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1957874216 197 TVIRLAGGENVLHD-AFSGYKPLSAEAALAAAPEVILVTQRNLEQLGGLDAVLERGALQATPAGQARRVLAMD 268
Cdd:pfam01497 159 DLLRILGIENIAAElSGSEYAPISFEAILSSNPDVIIVSGRDSFTKTGPEFVAANPLWAGLPAVKNGRVYTLP 231
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
37-299 |
2.97e-12 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 66.47 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 37 ARLISVDGAITEILYALGGEAQLVGVDTTSLYPDATEDIAKV--GYKRALSAEGILSLNPDrLLMTDDAGPPEVLEQIAR 114
Cdd:PRK09534 61 ERVVTLNPSAAQTMWELGARDRVVGVTQYASYLDGAEERTNVsgGQPFGVNVEAVVGLDPD-LVLAPNAVAGDTVTRLRE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 115 AGVDTHPIPDTPSVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATERSSKRPRLLFLLhigsGNDMAAGRDTA 194
Cdd:PRK09534 140 AGITVFHFPAATSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDDRPRVLYPL----GDGYTAGGNTF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 195 ADTVIRLAGGENVLHDA-FSGYKPLSAEAALAAAPEVILVTQRNleqlgglDAVLERGALQATPAGQARRVLAMDGPLLL 273
Cdd:PRK09534 216 IGALIEAAGGHNVAADAtTDGYPQLSEEVIVQQDPDVIVVATAS-------ALVAETEPYASTTAGETGNVVTVNVNHIN 288
|
250 260
....*....|....*....|....*.
gi 1957874216 274 AFGPRLAVAAAQLASELGIIDEETDE 299
Cdd:PRK09534 289 QPAPRIVESMATMATAFHNTTTNDTL 314
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
14-290 |
1.71e-97 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 288.63 E-value: 1.71e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 14 AAIGLLWCASALLAETGETSAQTARLISVDGAITEILYALGGEAQLVGVDTTSLYPDATEDIAKVGYKRALSAEGILSLN 93
Cdd:COG4558 5 ALALLLLALAALAAGASVAAAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGILSLK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 94 PDRLLMTDDAGPPEVLEQIARAGVDTHPIPDTPSVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATERSSKRP 173
Cdd:COG4558 85 PTLVLASEGAGPPEVLDQLRAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAAIGKPP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 174 RLLFLLHIGSGNDMAAGRDTAADTVIRLAGGENVLhDAFSGYKPLSAEAALAAAPEVILVTQRNLEQLGGLDAVLERGAL 253
Cdd:COG4558 165 RVLFLLSRGGGRPMVAGRGTAADALIRLAGGVNAA-AGFEGYKPLSAEALIAAAPDVILVMTRGLESLGGVDGLLALPGL 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 1957874216 254 QATPAGQARRVLAMDGPLLLAFGPRLAVAAAQLASEL 290
Cdd:COG4558 244 AQTPAGKNKRIVAMDDLLLLGFGPRTPQAALALAQAL 280
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
38-269 |
2.80e-70 |
|
Hemin binding protein HutB. These proteins have been shown to function as initial receptors in ABC transport of hemin and hemoproteins in many eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238569 [Multi-domain] Cd Length: 235 Bit Score: 217.52 E-value: 2.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 38 RLISVDGAITEILYALGGEAQLVGVDTTSLYPDATEDIAKVGYKRALSAEGILSLNPDRLLMTDDAGPPEVLEQIARAGV 117
Cdd:cd01149 3 RIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEALDQLRAAGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 118 DTHPIPDTPSVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATERSSKRPRLLFLLHIGSGNDMAAGRDTAADT 197
Cdd:cd01149 83 PVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVLFLLSHGGGAAMAAGRNTAADA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1957874216 198 VIRLAGGENVLhDAFSGYKPLSAEAALAAAPEVILVTQRNLEQLGGLDAVLERGALQATPAGQARRVLAMDG 269
Cdd:cd01149 163 IIALAGAVNAA-AGFRGYKPLSAEALIAAQPDVILVMSRGLDAVGGVDGLLKLPGLAQTPAGRNKRILAMDD 233
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
38-290 |
3.77e-39 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 138.59 E-value: 3.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 38 RLISVDGAITEILYALGGEAQLVGVDTTSLY---PDATEDIAKVGYKRALSAEGILSLNPDRLLMTDDAGPPEVLEQIAR 114
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCdypELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 115 AGVDTHPIpDTPSVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATERSSKRPRLLFLLHIGSGNdMAAGRDTA 194
Cdd:COG0614 82 IGIPVVVL-DPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPL-YTAGGGSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 195 ADTVIRLAGGENVLHDAFSGYKPLSAEAALAAAPEVILVTQRNLEQLGG---LDAVLERGALQATPAGQARRVLAMDGPL 271
Cdd:COG0614 160 IGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAeeaLEALLADPGWQSLPAVKNGRVYVVPGDL 239
|
250
....*....|....*....
gi 1957874216 272 LLAFGPRLAVAAAQLASEL 290
Cdd:COG0614 240 LSRPGPRLLLALEDLAKAL 258
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
38-216 |
1.38e-34 |
|
Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238563 [Multi-domain] Cd Length: 195 Bit Score: 124.31 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 38 RLISVDGAITEILYALGGEAQLVGVDTTSLYPDATEDIAKVGYKRALSAEGILSLNPDrLLMTDDAGPPEVLEQIARAGV 117
Cdd:cd01143 5 RIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPD-LVIVSSSSLAELLEKLKDAGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 118 DTHPIPDTPSVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATErssKRPRLLFLLHIGSGNDMAAGRDTAADT 197
Cdd:cd01143 84 PVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGK---TIKKSKVYIEVSLGGPYTAGKNTFINE 160
|
170
....*....|....*....
gi 1957874216 198 VIRLAGGENVLHDAfSGYK 216
Cdd:cd01143 161 LIRLAGAKNIAADS-GGWP 178
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
40-268 |
4.90e-28 |
|
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 426291 [Multi-domain] Cd Length: 233 Bit Score: 108.22 E-value: 4.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 40 ISVDGAITEILYALGGEAQLVGVDTTSLYP---DATEDIAKVGYKRALSAEGILSLNPDRLLMtDDAGPPEVLEQIARAG 116
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPlkaDAVAAIVKVGAYGEINVERLAALKPDLVIL-STGYLTDEAEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 117 VDTHPIPDTPSVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATERSSKRPRLLFLLHIGSGNdMAAGRDTAAD 196
Cdd:pfam01497 80 IPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGY-VVAGSNTYIG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1957874216 197 TVIRLAGGENVLHD-AFSGYKPLSAEAALAAAPEVILVTQRNLEQLGGLDAVLERGALQATPAGQARRVLAMD 268
Cdd:pfam01497 159 DLLRILGIENIAAElSGSEYAPISFEAILSSNPDVIIVSGRDSFTKTGPEFVAANPLWAGLPAVKNGRVYTLP 231
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
38-287 |
2.10e-26 |
|
Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238564 [Multi-domain] Cd Length: 245 Bit Score: 104.30 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 38 RLISVDGAITEILYALGGEAQLVGVDTTSLYPDATEDIAKVGYKRALSAEGILSLNPDRLLMTDDAGPPEVLEQIARAGV 117
Cdd:cd01144 2 RIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 118 DTHPIPDTpSVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATeRSSKRPRLLFLLhigsGND--MAAGRDTAA 195
Cdd:cd01144 82 PVLVSEPQ-TLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQY-ASKPPPRVFYQE----WIDplMTAGGDWVP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 196 DtVIRLAGGENVLHDAFSGYKPLSAEAALAAAPEVILV----TQRNLEQLGGldavleRGALQATPAGQARRVLAMDGPL 271
Cdd:cd01144 156 E-LIALAGGVNVFADAGERSPQVSWEDVLAANPDVIVLspcgFGFTPAILRK------EPAWQALPAVRNGRVYAVDGNW 228
|
250
....*....|....*.
gi 1957874216 272 LLAFGPRLAVAAAQLA 287
Cdd:cd01144 229 YFRPSPRLVDGLEQLA 244
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
38-177 |
4.21e-18 |
|
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.
Pssm-ID: 238347 [Multi-domain] Cd Length: 148 Bit Score: 79.53 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 38 RLISVDGAITEILYALGGEAQLVGVDTTSLYPD----ATEDIAKVGYKRALSAEGILSLNPDrLLMTDDAGPPEVLEQIA 113
Cdd:cd00636 2 RVVALDPGATELLLALGGDDKPVGVADPSGYPPeakaLLEKVPDVGHGYEPNLEKIAALKPD-LIIANGSGLEAWLDKLS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1957874216 114 RAGVDTHPIPDT--PSVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATERSSKRPRLLF 177
Cdd:cd00636 81 KIAIPVVVVDEAseLSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLV 146
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
38-287 |
1.17e-15 |
|
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238568 [Multi-domain] Cd Length: 284 Bit Score: 75.45 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 38 RLISVDGAITEILYALGGEAQLVGvdTTSLYPDATEDIAKVGYK------RALSAEGILSLNPDRLLMTDDAG-PPEVL- 109
Cdd:cd01148 20 RVVSNDQNTTEMMLALGLQDRMVG--TAGIDNKDLPELKAKYDKvpelakKYPSKETVLAARPDLVFGGWSYGfDKGGLg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 110 --EQIARAGVDTHPIPDT-------PSVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATERSSKRPRLlFLLH 180
Cdd:cd01148 98 tpDSLAELGIKTYILPEScgqrrgeATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDGKKVAV-FVYD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 181 IGSGNDMAAGRDTAADTVIRLAGGENVLHDAFSGYKPLSAEAALAAAPEVILV----TQRNLEQLggLDAVLERGALQAT 256
Cdd:cd01148 177 SGEDKPFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVIidygDQNAAEQK--IKFLKENPALKNV 254
|
250 260 270
....*....|....*....|....*....|.
gi 1957874216 257 PAGQARRVLAMDGPLLLAfGPRLAVAAAQLA 287
Cdd:cd01148 255 PAVKNNRFIVLPLAEATP-GIRNVDAIEKLA 284
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
34-211 |
3.50e-15 |
|
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238562 [Multi-domain] Cd Length: 289 Bit Score: 74.31 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 34 AQTARLISVDGAITEILYALGGEAQLVGVDTTS--------LYPDaTEDIAKVGYKRALSAEGILSLNPDRLLMTDDAGP 105
Cdd:cd01142 22 DEVKRIAALWGAGNAVVAALGGGKLIVATTSTVqqepwlyrLAPS-LENVATGGTGNDVNIEELLALKPDVVIVWSTDGK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 106 pEVLEQIARAgvdthpIP-DTPSVAGLHE---TIAAVAEVLDRTEAGAALSAQLDDELAQLEAATER--SSKRPRLLfll 179
Cdd:cd01142 101 -EAGKAVLRL------LNaLSLRDAELEEvklTIALLGELLGRQEKAEALVAYFDDNLAYVAARTKKlpDSERPRVY--- 170
|
170 180 190
....*....|....*....|....*....|..
gi 1957874216 180 HIGSGNDMAAGRDTAADTVIRLAGGENVLHDA 211
Cdd:cd01142 171 YAGPDPLTTDGTGSITNSWIDLAGGINVASEA 202
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
37-299 |
2.97e-12 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 66.47 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 37 ARLISVDGAITEILYALGGEAQLVGVDTTSLYPDATEDIAKV--GYKRALSAEGILSLNPDrLLMTDDAGPPEVLEQIAR 114
Cdd:PRK09534 61 ERVVTLNPSAAQTMWELGARDRVVGVTQYASYLDGAEERTNVsgGQPFGVNVEAVVGLDPD-LVLAPNAVAGDTVTRLRE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 115 AGVDTHPIPDTPSVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATERSSKRPRLLFLLhigsGNDMAAGRDTA 194
Cdd:PRK09534 140 AGITVFHFPAATSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDDRPRVLYPL----GDGYTAGGNTF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 195 ADTVIRLAGGENVLHDA-FSGYKPLSAEAALAAAPEVILVTQRNleqlgglDAVLERGALQATPAGQARRVLAMDGPLLL 273
Cdd:PRK09534 216 IGALIEAAGGHNVAADAtTDGYPQLSEEVIVQQDPDVIVVATAS-------ALVAETEPYASTTAGETGNVVTVNVNHIN 288
|
250 260
....*....|....*....|....*.
gi 1957874216 274 AFGPRLAVAAAQLASELGIIDEETDE 299
Cdd:PRK09534 289 QPAPRIVESMATMATAFHNTTTNDTL 314
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
38-211 |
1.72e-09 |
|
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238567 [Multi-domain] Cd Length: 262 Bit Score: 57.34 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 38 RLISVDGAITEILYALGGEAQLVGVDTTSLYPDAT------------EDIAKVGYKRALSAEGILSLNPDRLLMTDDAGP 105
Cdd:cd01147 7 RVVAAGPGALRLLYALAAPDKIVGVDDAEKSDEGRpyflaspelkdlPVIGRGGRGNTPNYEKIAALKPDVVIDVGSDDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 106 PEVLEQI-ARAGvdthpIP----DTP-SVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATE--RSSKRPRLLF 177
Cdd:cd01147 87 TSIADDLqKKTG-----IPvvvlDGGdSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKdiPDEEKPTVYF 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1957874216 178 LlhiGSGNDMAAGRDTAADT---VIRLAGGENVLHDA 211
Cdd:cd01147 162 G---RIGTKGAAGLESGLAGsieVFELAGGINVADGL 195
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
27-204 |
2.37e-09 |
|
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238561 [Multi-domain] Cd Length: 186 Bit Score: 55.89 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 27 AETGETSAQtaRLISVDGAITEILYALGGEAQLVGVDTTSlYPDATEDIAK-----VGYKRALSAEGILSLNPDrLLMTD 101
Cdd:cd01141 1 AKTIKVPPK--RIVVLSPTHVDLLLALDKADKIVGVSASA-YDLNTPAVKEridiqVGPTGSLNVELIVALKPD-LVILY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 102 DAGPPEVLEQIA-RAGVDTHPIPDTPSVAGLHETIAAVAEvldrtEAGAALSAQLDDELAQLE------AATERSSKRPR 174
Cdd:cd01141 77 GGFQAQTILDKLeQLGIPVLYVNEYPSPLGRAEWIKFAAA-----FYGVGKEDKADEAFAQIAgryrdlAKKVSNLNKPT 151
|
170 180 190
....*....|....*....|....*....|
gi 1957874216 175 LLFLLHIGSGNDMAAGRDTAADtVIRLAGG 204
Cdd:cd01141 152 VAIGKPVKGLWYMPGGNSYVAK-MLRDAGG 180
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
14-211 |
4.56e-09 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 56.23 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 14 AAIGLLWCASALLAetgetSAQtaRLISVDGAITEILYALG-GEaqlVGVDTTSLYPDATEDIAKVGYKRALSAEGILSL 92
Cdd:PRK03379 2 ALVALLFLAPLWLN-----AAP--RVITLSPANTELAFAAGiTP---VGVSSYSDYPPQAKKIEQVATWQGMNLERIVAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 93 NPDRLLMTDDAGPPEVLEQIARAGVdthPI--PDTPSVAGLHETIAAVAEVLDRTEAGAALSAQLDDELAQLEAATERSS 170
Cdd:PRK03379 72 KPDLVLAWRGGNAERQVDQLASLGI---KVmwVDATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKP 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1957874216 171 KRPrllFLLHIGSGNDMAAGRDTAADTVIRLAGGENVLHDA 211
Cdd:PRK03379 149 KKR---VFLQFGTNPLFTSGKHSIQSQVLSLCGGENIFADS 186
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
3-179 |
7.83e-04 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 40.38 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 3 PRKRLLTTVtgAAIGLLWCASALLAetgeTSAQTARLISVDGAITEILYALG----GEAQL----VGVDTTSLyPDATED 74
Cdd:PRK10576 5 SRRRLLTAM--ALSPLLWQMNTAAA----AAIDPNRIVALEWLPVELLLALGvtpyGVADThnyrLWVSEPAL-PDSVID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957874216 75 iakVGYKRALSAEGILSLNPDRLLMTDDAGP-PEVLEQIARA-GVDTHPiPDTPsVAGLHETIAAVAEVLDRTEAGAALS 152
Cdd:PRK10576 78 ---VGLRTEPNLELLTQMKPSLILWSAGYGPsPEKLARIAPGrGFAFSD-GKKP-LAVARKSLVELAQRLNLEAAAETHL 152
|
170 180
....*....|....*....|....*..
gi 1957874216 153 AQLDDELAQLEAATERSSKRPRLLFLL 179
Cdd:PRK10576 153 AQFDDFIASAKPRLAGRGQRPLLLTSL 179
|
|
| |
